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Träfflista för sökning "hsv:(NATURVETENSKAP) hsv:(Biologi) hsv:(Biokemi och molekylärbiologi) srt2:(1970-1979)"

Sökning: hsv:(NATURVETENSKAP) hsv:(Biologi) hsv:(Biokemi och molekylärbiologi) > (1970-1979)

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  • Mosbach, Klaus, et al. (författare)
  • Preparation and application of polymer-entrapped enzymes and microorganisms in microbial transformation processes with special reference to steroid 11-β-hydroxylation and Δ1-dehydrogenation
  • 1970
  • Ingår i: Biotechnology and Bioengineering. - : Wiley. - 1097-0290 .- 0006-3592. ; 12:1, s. 19-27
  • Tidskriftsartikel (refereegranskat)abstract
    • Fungal cells from Curvularia lunata were entrapped in a crosslinked polyacrylamide gel. The gel-cells obtained as granules were applied in the microbial transformation of Reichstein compound S leading to cortisol through an 11-β-hydroxylation step. Some kinetic studies of this conversion using gel-cells were carried out. In addition, it was shown that gel-cell granules which had lost part of their 11-β-hydroxylase activity on storage could be reactivated yielding preparations with increased activity. From Corynebacterium simplex a steroid dehydrogenase catalyzing the Δ1- dehydrogenation of cortisol leading to prednisolone was isolated and partially purified. The preparation was entrapped in a crosslinked polyacrylamide gel and the gel-enzyme granules obtained used in steroid dehydrogenation processes.
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  • Brodelius, Peter, et al. (författare)
  • Determination of Dissociation Constants for Binary Dehydrogenase-Coenzyme Complexes by (Bio)Affinity Chromatography on an Immobilized AMP-Analogue
  • 1976
  • Ingår i: Analytical biochemistry. - : Elsevier BV. - 0003-2697. ; 72:1-2, s. 629-636
  • Tidskriftsartikel (refereegranskat)abstract
    • Various alcohol and lactate dehydrogenases were adsorbed to an affinity column of immobilized N6-(6-aminohexyl)-AMP and subsequently eluted with gradients of coenzymes or coenzyme fragments. A linear relation was observed between the eluting concentration of nucleotide and the reported dissociation constants for the corresponding binary enzyme-nucleotide complexes. This relation has been utilized to determine unknown dissociation constants by affinity chromatography. The method presented can also be utilized for the estimation of dissociation constants betweendehydrogenases and coenzyme analogues. 
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  • Brodelius, Peter, et al. (författare)
  • Studies of Bovine Liver Glutamate Dehydrogenase by Analytical Affinity Chromatography on Immobilized AMP Analogs
  • 1979
  • Ingår i: Archives of Biochemistry and Biophysics. - : Elsevier BV. - 0003-9861. ; 194:2, s. 449-456
  • Tidskriftsartikel (refereegranskat)abstract
    • Bovine liver glutamate dehydrogenase has been studied by analytical affinity chromatography on two immobilized AMP analogs, i.e., N6-(6-aminohexyl)-AMP and 8-(6-aminohexyl)-amino-AMP. The existence of various enzyme-coenzyme and enzyme-effector complexes has been verified. Also the cooperative formation of two ternary complexes, i.e., glutamic dehydrogenase (GHD)-NADP-glutamate and GDH-ADP-leucine, has been shown. The results of this study have been rationalized by the “ligand exclusion theory.” which has been proposed for the regulation of the glutamic dehydrogenase. It has been shown that the active site and the ADP-binding effector site are oriented close to each other on the enzyme. Furthermore, the data suggest that the adenylic site is not identical to the nonactive coenzyme binding site. A mechanism based on electrostatic interactions is suggested for the cooperative binding of oxidized coenzyme and substrate. Dissociation constants for complexes between the enzyme and two coenzyme fragments (P-ADPR and 2′,5′-ADP) have been estimated.
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